BGLK_LISIN
ID BGLK_LISIN Reviewed; 294 AA.
AC Q926Y3;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Beta-glucoside kinase;
DE EC=2.7.1.85;
GN Name=bglK; OrderedLocusNames=lin2907;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=12110692; DOI=10.1074/jbc.m206397200;
RA Thompson J., Lichtenthaler F.W., Peters S., Pikis A.;
RT "Beta-glucoside kinase (BglK) from Klebsiella pneumoniae. Purification,
RT properties, and preparative synthesis of 6-phospho-beta-D-glucosides.";
RL J. Biol. Chem. 277:34310-34321(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of cellobiose to
CC produce cellobiose-6'-P. May have a dual role of kinase and
CC transcriptional regulator of the cellobiose-PTS operon.
CC {ECO:0000269|PubMed:12110692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-cellobiose = 6-phospho-beta-D-glucosyl-(1->4)-D-
CC glucose + ADP + H(+); Xref=Rhea:RHEA:21944, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17057, ChEBI:CHEBI:30616, ChEBI:CHEBI:58312,
CC ChEBI:CHEBI:456216; EC=2.7.1.85;
CC Evidence={ECO:0000269|PubMed:12110692};
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; AL596174; CAC98132.1; -; Genomic_DNA.
DR PIR; AD1795; AD1795.
DR RefSeq; WP_010991440.1; NC_003212.1.
DR AlphaFoldDB; Q926Y3; -.
DR SMR; Q926Y3; -.
DR STRING; 272626.lin2907; -.
DR EnsemblBacteria; CAC98132; CAC98132; CAC98132.
DR GeneID; 61171033; -.
DR KEGG; lin:lin2907; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_2_9; -.
DR OMA; ANYDAHD; -.
DR OrthoDB; 1130699at2; -.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047700; F:beta-glucoside kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..294
FT /note="Beta-glucoside kinase"
FT /id="PRO_0000390477"
FT BINDING 5..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 32210 MW; 5AF6AEFC11CB5E29 CRC64;
MKIAAFDIGG TALKMGVVLP HGEIILTKSA EIIASDGDQI LAEMKLFLAE NTDVTGIAVS
APGYVNPKTG LITMGGAIRR FDNFNLKEWL EAETGLPVAI ENDANCALLA EKWLGKGQDL
DDFLCLTIGT GIGGGIFSNG ALVRGGRFRA GEFGYMFSER PGAFRPGKYT LNETTTMLVL
RRQYAQLTGR PLKEITGEEI FANYDAHDPI SERLINEFYT GICTGLYNLI YLFDPTHIFI
GGGITSRPTF ITELKHHMAS FGLRDTIIET ATHKNQAGLL GAVYHFLQEE NRHE